|
Name |
Accession |
Description |
Interval |
E-value |
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
24-385 |
0e+00 |
|
This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
Pssm-ID: 119351 [Multi-domain] Cd Length: 362 Bit Score: 643.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 24 LVCYFTNWAQYRQGEARFLPKDVDPSLCTHLIYAFAGMTN--HQLSTIEWND--ETLYQEFNGRKKMNPKLKTLLAIGGW 99
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPdgNIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 100 NFGTQRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSPAIDKERFTALVQDLANAFQQEAqtsgkERLL 179
Cdd:cd02872 81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDKENFVTLLKELREAFEPEA-----PRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 180 LSAAVPAGRTYVDAGYEVDKIARNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAASLNVDAAVQMWLQKGTPASK 259
Cdd:cd02872 156 LTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 260 LILGMPTYGRSFTLASPSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSW--KGATKQRIQDQEVPYIFRDNQWVGFDDV 337
Cdd:cd02872 236 LVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFlkSGWTVVWDDEQKVPYAYKGNQWVGYDDE 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622828392 338 ESFKTKVSYLKQKGLGGAMVWALDLDDFAGFsCDQGRYPLIQTLRREL 385
Cdd:cd02872 316 ESIALKVQYLKSKGLGGAMVWSIDLDDFRGT-CGQGKYPLLNAINRAL 362
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
23-363 |
5.43e-156 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 445.58 E-value: 5.43e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 23 KLVCYFTNWAQYRQgeaRFLPKDVDPSLCTHLIYAFAGMTNHQLSTI--EWNDETLYQEFNGRKKMNPKLKTLLAIGGWN 100
Cdd:smart00636 1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVTIgdEWADIGNFGQLKALKKKNPGLKVLLSIGGWT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 101 FGtQRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSpaiDKERFTALVQDLANAFQQEAQTsgKERLLL 180
Cdd:smart00636 78 ES-DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGD---DRENYTALLKELREALDKEGAE--GKGYLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 181 SAAVPAGRTYVDAGYE-VDKIARNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAaasLNVDAAVQMWLQKGTPASK 259
Cdd:smart00636 152 TIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPEK---YNVDYAVKYYLCKGVPPSK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 260 LILGMPTYGRSFTLASPSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQEVPYIFRDN--QWVGFDDV 337
Cdd:smart00636 229 LVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLLGATVVYDDTAKAPYAYNPGtgQWVSYDDP 308
|
330 340
....*....|....*....|....*.
gi 1622828392 338 ESFKTKVSYLKQKGLGGAMVWALDLD 363
Cdd:smart00636 309 RSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
23-363 |
2.24e-128 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 374.48 E-value: 2.24e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 23 KLVCYFTNWAQYRQGEArflpkdVDPSLCTHLIYAFAGMT--NHQLSTIEWnDETLYQEFNG-RKKMNPKLKTLLAIGGW 99
Cdd:pfam00704 1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIDgsDGTLFIGDW-DLGNFEQLKKlKKQKNPGVKVLLSIGGW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 100 NFGTqRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSpaiDKERFTALVQDLANAFQQEaqtSGKERLL 179
Cdd:pfam00704 74 TDST-GFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGNPE---DKENYDLLLRELRAALDEA---KGGKKYL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 180 LSAAVPAGRTYVDAGYEVDKIARNLDFVNLMAYDFHGSWEKVTGHNSPLYkrqeesgAAASLNVDAAVQMWLQKGTPASK 259
Cdd:pfam00704 147 LSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY-------GGGSYNVDYAVKYYLKQGVPASK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 260 LILGMPTYGRSFTLASPSDTrvgapatgsgtpgpfTKEGGMLAYYEVCSW-KGATKQRIQD--QEVPYIFRDNQWVGFDD 336
Cdd:pfam00704 220 LVLGVPFYGRSWTLVNGSGN---------------TWEDGVLAYKEICNLlKDNGATVVWDdvAKAPYVYDGDQFITYDD 284
|
330 340
....*....|....*....|....*..
gi 1622828392 337 VESFKTKVSYLKQKGLGGAMVWALDLD 363
Cdd:pfam00704 285 PRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
23-367 |
3.09e-111 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 333.80 E-value: 3.09e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 23 KLVCYFTNWAQYRQGearFLPKDVDPSLCTHLIYAFA----------GMTNHQLS----TIEWND--ETLYQEFNGRKKM 86
Cdd:COG3325 20 RVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFAnvdpdgkcsvGDAWAKPSvdgaADDWDQplKGNFNQLKKLKAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 87 NPKLKTLLAIGGWNfGTQRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSPAI-----DKERFTALVQD 161
Cdd:COG3325 97 NPNLKVLISIGGWT-WSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNvyrpeDKANFTALLKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 162 LANAFQQEAQTSGKeRLLLSAAVPAGRTYVDaGYEVDKIARNLDFVNLMAYDFHGSWEKVTGHNSPLYkRQEESGAAASL 241
Cdd:COG3325 176 LRAQLDALGAETGK-HYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLY-DSPKDPEAQGY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 242 NVDAAVQMWLQKGTPASKLILGMPTYGRSFTLASPSDTRVGAPATGsgtPGPFTKEGGMLAYYE----VCSWKGATKQRI 317
Cdd:COG3325 253 SVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATG---PAPGTWEAGVNDYKDlkalYLGSNGYTRYWD 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622828392 318 QDQEVPYIFRDN--QWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAG 367
Cdd:COG3325 330 DVAKAPYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADG 381
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
419-466 |
5.47e-14 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 65.93 E-value: 5.47e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1622828392 419 FCQGKADGLYPNPRERSSFYSCAGGRLFQQSCPAGLVFSSSCKCCTWN 466
Cdd:smart00494 2 ECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
420-465 |
1.05e-11 |
|
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.
Pssm-ID: 426342 [Multi-domain] Cd Length: 53 Bit Score: 59.73 E-value: 1.05e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622828392 420 CQGKADGLYPNPRERSSFYSCAGGRLFQQSCPAGLVFSSSCKCCTW 465
Cdd:pfam01607 1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
24-385 |
0e+00 |
|
This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
Pssm-ID: 119351 [Multi-domain] Cd Length: 362 Bit Score: 643.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 24 LVCYFTNWAQYRQGEARFLPKDVDPSLCTHLIYAFAGMTN--HQLSTIEWND--ETLYQEFNGRKKMNPKLKTLLAIGGW 99
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPdgNIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 100 NFGTQRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSPAIDKERFTALVQDLANAFQQEAqtsgkERLL 179
Cdd:cd02872 81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDKENFVTLLKELREAFEPEA-----PRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 180 LSAAVPAGRTYVDAGYEVDKIARNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAASLNVDAAVQMWLQKGTPASK 259
Cdd:cd02872 156 LTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 260 LILGMPTYGRSFTLASPSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSW--KGATKQRIQDQEVPYIFRDNQWVGFDDV 337
Cdd:cd02872 236 LVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFlkSGWTVVWDDEQKVPYAYKGNQWVGYDDE 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622828392 338 ESFKTKVSYLKQKGLGGAMVWALDLDDFAGFsCDQGRYPLIQTLRREL 385
Cdd:cd02872 316 ESIALKVQYLKSKGLGGAMVWSIDLDDFRGT-CGQGKYPLLNAINRAL 362
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
23-363 |
5.43e-156 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 445.58 E-value: 5.43e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 23 KLVCYFTNWAQYRQgeaRFLPKDVDPSLCTHLIYAFAGMTNHQLSTI--EWNDETLYQEFNGRKKMNPKLKTLLAIGGWN 100
Cdd:smart00636 1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVTIgdEWADIGNFGQLKALKKKNPGLKVLLSIGGWT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 101 FGtQRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSpaiDKERFTALVQDLANAFQQEAQTsgKERLLL 180
Cdd:smart00636 78 ES-DNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRGD---DRENYTALLKELREALDKEGAE--GKGYLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 181 SAAVPAGRTYVDAGYE-VDKIARNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAaasLNVDAAVQMWLQKGTPASK 259
Cdd:smart00636 152 TIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPEK---YNVDYAVKYYLCKGVPPSK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 260 LILGMPTYGRSFTLASPSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQEVPYIFRDN--QWVGFDDV 337
Cdd:smart00636 229 LVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLLGATVVYDDTAKAPYAYNPGtgQWVSYDDP 308
|
330 340
....*....|....*....|....*.
gi 1622828392 338 ESFKTKVSYLKQKGLGGAMVWALDLD 363
Cdd:smart00636 309 RSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
23-363 |
2.24e-128 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 374.48 E-value: 2.24e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 23 KLVCYFTNWAQYRQGEArflpkdVDPSLCTHLIYAFAGMT--NHQLSTIEWnDETLYQEFNG-RKKMNPKLKTLLAIGGW 99
Cdd:pfam00704 1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIDgsDGTLFIGDW-DLGNFEQLKKlKKQKNPGVKVLLSIGGW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 100 NFGTqRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSpaiDKERFTALVQDLANAFQQEaqtSGKERLL 179
Cdd:pfam00704 74 TDST-GFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGNPE---DKENYDLLLRELRAALDEA---KGGKKYL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 180 LSAAVPAGRTYVDAGYEVDKIARNLDFVNLMAYDFHGSWEKVTGHNSPLYkrqeesgAAASLNVDAAVQMWLQKGTPASK 259
Cdd:pfam00704 147 LSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLY-------GGGSYNVDYAVKYYLKQGVPASK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 260 LILGMPTYGRSFTLASPSDTrvgapatgsgtpgpfTKEGGMLAYYEVCSW-KGATKQRIQD--QEVPYIFRDNQWVGFDD 336
Cdd:pfam00704 220 LVLGVPFYGRSWTLVNGSGN---------------TWEDGVLAYKEICNLlKDNGATVVWDdvAKAPYVYDGDQFITYDD 284
|
330 340
....*....|....*....|....*..
gi 1622828392 337 VESFKTKVSYLKQKGLGGAMVWALDLD 363
Cdd:pfam00704 285 PRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
23-367 |
3.09e-111 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 333.80 E-value: 3.09e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 23 KLVCYFTNWAQYRQGearFLPKDVDPSLCTHLIYAFA----------GMTNHQLS----TIEWND--ETLYQEFNGRKKM 86
Cdd:COG3325 20 RVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFAnvdpdgkcsvGDAWAKPSvdgaADDWDQplKGNFNQLKKLKAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 87 NPKLKTLLAIGGWNfGTQRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSPAI-----DKERFTALVQD 161
Cdd:COG3325 97 NPNLKVLISIGGWT-WSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNvyrpeDKANFTALLKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 162 LANAFQQEAQTSGKeRLLLSAAVPAGRTYVDaGYEVDKIARNLDFVNLMAYDFHGSWEKVTGHNSPLYkRQEESGAAASL 241
Cdd:COG3325 176 LRAQLDALGAETGK-HYLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLY-DSPKDPEAQGY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 242 NVDAAVQMWLQKGTPASKLILGMPTYGRSFTLASPSDTRVGAPATGsgtPGPFTKEGGMLAYYE----VCSWKGATKQRI 317
Cdd:COG3325 253 SVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATG---PAPGTWEAGVNDYKDlkalYLGSNGYTRYWD 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622828392 318 QDQEVPYIFRDN--QWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAG 367
Cdd:COG3325 330 DVAKAPYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADG 381
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
25-363 |
7.46e-101 |
|
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.
Pssm-ID: 119365 [Multi-domain] Cd Length: 322 Bit Score: 304.55 E-value: 7.46e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 25 VCYFTNWAQYrqGEARFLPKDVDPSLCTHLIYAFAGM---TNHQLSTIEWNDETLY-----------------QEFNGRK 84
Cdd:cd06548 2 VGYFTNWGIY--GRNYFVTDDIPADKLTHINYAFADIdgdGGVVTSDDEAADEAAQsvdggadtddqplkgnfGQLRKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 85 KMNPKLKTLLAIGGWNFGtQRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSPAI-----DKERFTALV 159
Cdd:cd06548 80 QKNPHLKILLSIGGWTWS-GGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGNvarpeDKENFTLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 160 QDLANAFQQEAQTSGKeRLLLSAAVPAGRTYVDAGyEVDKIARNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESgaAA 239
Cdd:cd06548 159 KELREALDALGAETGR-KYLLTIAAPAGPDKLDKL-EVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYASPADP--PG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 240 SLNVDAAVQMWLQKGTPASKLILGMPTYGRSftlaspsdtrvgapatgsgtpgpftkeggmlayyevcsWKGATKQRIQD 319
Cdd:cd06548 235 GYSVDAAVNYYLSAGVPPEKLVLGVPFYGRG--------------------------------------WTGYTRYWDEV 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622828392 320 QEVPYIF--RDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLD 363
Cdd:cd06548 277 AKAPYLYnpSTKTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
23-385 |
7.94e-80 |
|
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects that include at least five members, some of which are encoded by genes in a tight cluster. The IDGF's have an eight-stranded alpha/beta barrel fold and are related to the glycosyl hydrolase family 18 (GH18) chitinases, but they have an amino acid substitution known to abolish chitinase catalytic activity. IDGFs may have evolved from chitinases to gain new functions as growth factors, interacting with cell surface glycoproteins involved in growth-promoting processes.
Pssm-ID: 119352 [Multi-domain] Cd Length: 413 Bit Score: 253.78 E-value: 7.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 23 KLVCYFTNWAQYRQGEARFLPKDVDPSL--CTHLIYAFAGMT--NHQLSTIEWN---DETLYQEFNGRKKMNPKLKTLLA 95
Cdd:cd02873 1 KLVCYYDSKSYLREGLAKMSLEDLEPALqfCTHLVYGYAGIDadTYKIKSLNEDldlDKSHYRAITSLKRKYPHLKVLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 96 IGGWNF-----GTQRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYP-----------GS---------RGSPAI 150
Cdd:cd02873 81 VGGDRDtdeegENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPknkpkkvrgtfGSawhsfkklfTGDSVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 151 D------KERFTALVQDLANAFQQEAQtsgkerlLLSAAV-PagrtYVDAG--YEVDKIARNLDFVNLMAYDFHGSWE-- 219
Cdd:cd02873 161 DekaaehKEQFTALVRELKNALRPDGL-------LLTLTVlP----HVNSTwyFDVPAIANNVDFVNLATFDFLTPERnp 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 220 KVTGHNSPLYKRQEESgaaASLNVDAAVQMWLQKGTPASKLILGMPTYGRSFTLASPS-DTRV--GAPATGSGTPGPFTK 296
Cdd:cd02873 230 EEADYTAPIYELYERN---PHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKLTKDSgITGVppVLETDGPGPAGPQTK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 297 EGGMLAYYEVCS-------WKGATK--QRIQDQEV---PYIFR---DNQ----WVGFDDVESFKTKVSYLKQKGLGGAMV 357
Cdd:cd02873 307 TPGLLSWPEICSklpnpanLKGADAplRKVGDPTKrfgSYAYRpadENGehgiWVSYEDPDTAANKAGYAKAKGLGGVAL 386
|
410 420
....*....|....*....|....*...
gi 1622828392 358 WALDLDDFAGfSCDQGRYPLIQTLRREL 385
Cdd:cd02873 387 FDLSLDDFRG-QCTGDKFPILRSAKYRL 413
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
41-364 |
9.12e-79 |
|
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the chitin-binding domain present in other GH18 enzymes. The GH18 domain of the class V chitinases has endochitinase activity in some cases and no catalytic activity in others. Included in this family is a lectin found in black locust (Robinia pseudoacacia) bark, which binds chitin but lacks chitinase activity. Also included is a chitinase-related receptor-like kinase (CHRK1) from tobacco (Nicotiana tabacum), with an N-terminal GH18 domain and a C-terminal kinase domain, which is thought to be part of a plant signaling pathway. The GH18 domain of CHRK1 is expressed extracellularly where it binds chitin but lacks chitinase activity.
Pssm-ID: 119358 [Multi-domain] Cd Length: 299 Bit Score: 247.28 E-value: 9.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 41 FLPKDVDPSLCTHLIYAFAGM--TNHQLsTIEWNDETLYQEF-NGRKKMNPKLKTLLAIGGWNFGTQRFTDMVATANNRQ 117
Cdd:cd02879 16 FPPSNIDSSLFTHLFYAFADLdpSTYEV-VISPSDESEFSTFtETVKRKNPSVKTLLSIGGGGSDSSAFAAMASDPTARK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 118 TFVNSAIRFLRKYGFDGLDLDWEYPgsrgSPAIDKERFTALVQDLANAFQQEAQTSGKERLLLSAAVPAGRTYVDAG--- 194
Cdd:cd02879 95 AFINSSIKVARKYGFDGLDLDWEFP----SSQVEMENFGKLLEEWRAAVKDEARSSGRPPLLLTAAVYFSPILFLSDdsv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 195 -YEVDKIARNLDFVNLMAYDFHGSWEK-VTGHNSPLYKRqeesgaAASLNVDAAVQMWLQKGTPASKLILGMPTYGRSFT 272
Cdd:cd02879 171 sYPIEAINKNLDWVNVMAYDYYGSWESnTTGPAAALYDP------NSNVSTDYGIKSWIKAGVPAKKLVLGLPLYGRAWT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 273 LaspSDTRVGapatgsgtpgpftkeggmlayyevcswkgatkqriqdqeVPYIFRDNQWVGFDDVESFKTKVSYLKQKGL 352
Cdd:cd02879 245 L---YDTTTV---------------------------------------SSYVYAGTTWIGYDDVQSIAVKVKYAKQKGL 282
|
330
....*....|..
gi 1622828392 353 GGAMVWALDLDD 364
Cdd:cd02879 283 LGYFAWAVGYDD 294
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
24-213 |
2.03e-55 |
|
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
Pssm-ID: 119349 [Multi-domain] Cd Length: 210 Bit Score: 183.35 E-value: 2.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 24 LVCYFTNWAQYRqgeaRFLPKDVDPSLCTHLIYAFAGMT--NHQLSTIEWNDETLYQEFNGRKKMNPKLKTLLAIGGWNF 101
Cdd:cd00598 1 VICYYDGWSSGR----GPDPTDIPLSLCTHIIYAFAEISsdGSLNLFGDKSEEPLKGALEELASKKPGLKVLISIGGWTD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 102 GTqrFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSPaiDKERFTALVQDLANAFqqeaqtsGKERLLLS 181
Cdd:cd00598 77 SS--PFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPGAADNS--DRENFITLLRELRSAL-------GAANYLLT 145
|
170 180 190
....*....|....*....|....*....|..
gi 1622828392 182 AAVPAGRTYVDAGYEVDKIARNLDFVNLMAYD 213
Cdd:cd00598 146 IAVPASYFDLGYAYDVPAIGDYVDFVNVMTYD 177
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
43-363 |
7.90e-46 |
|
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
Pssm-ID: 119357 [Multi-domain] Cd Length: 345 Bit Score: 162.48 E-value: 7.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 43 PKDVDPSLCTHLIYAFAGMTnhqlSTIEWNDETLYQEFNGRKKMNpKLKTLLAIGGWNFGT-----QRFTDMVATANnRQ 117
Cdd:cd02878 20 VTQIDTSKYTHIHFAFANIT----SDFSVDVSSVQEQFSDFKKLK-GVKKILSFGGWDFSTspstyQIFRDAVKPAN-RD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 118 TFVNSAIRFLRKYGFDGLDLDWEYPGSRGSPAI------DKERFTALVQDLANAFQqeaqtSGKerlLLSAAVPAGRTYV 191
Cdd:cd02878 94 TFANNVVNFVNKYNLDGVDFDWEYPGAPDIPGIpagdpdDGKNYLEFLKLLKSKLP-----SGK---SLSIAAPASYWYL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 192 dAGYEVDKIARNLDFVNLMAYDFHGSWEkvtgHNSPLYKRQEESGAAASLNVD-----AAVQMWLQKGTPASKLILGMPT 266
Cdd:cd02878 166 -KGFPIKDMAKYVDYIVYMTYDLHGQWD----YGNKWASPGCPAGNCLRSHVNktetlDALSMITKAGVPSNKVVVGVAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 267 YGRSFTLASPSDTRVGAPATGSG-----TPGPFTKEGGMLAYYEVCSWKGATKQRIQDQEVP---YIFRDNQWVGFDDVE 338
Cdd:cd02878 241 YGRSFKMADPGCTGPGCTFTGPGsgaeaGRCTCTAGYGAISEIEIIDISKSKNKRWYDTDSDsdiLVYDDDQWVAYMSPA 320
|
330 340
....*....|....*....|....*
gi 1622828392 339 SFKTKVSYLKQKGLGGAMVWALDLD 363
Cdd:cd02878 321 TKAARIEWYKGLNFGGTSDWAVDLQ 345
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
109-364 |
1.15e-27 |
|
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.
Pssm-ID: 119353 [Multi-domain] Cd Length: 313 Bit Score: 112.36 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 109 MVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYpgsrgSPAIDKERFTALVQDLANAFQQEAQTsgkerlLLSAAVPA-- 186
Cdd:cd02874 81 VLSNPEARQRLINNILALAKKYGYDGVNIDFEN-----VPPEDREAYTQFLRELSDRLHPAGYT------LSTAVVPKts 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 187 ----GRTYvdAGYEVDKIARNLDFVNLMAYDFHGSWekvtghnSPlykrqeeSGAAASLN-----VDAAV-QMwlqkgtP 256
Cdd:cd02874 150 adqfGNWS--GAYDYAAIGKIVDFVVLMTYDWHWRG-------GP-------PGPVAPIGwvervLQYAVtQI------P 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 257 ASKLILGMPTYGRSFTLASPSDTRVGApatgsgtpgpftkeggmLAYYEVCSWK---GATKQRIQDQEVPYIF-RDNQ-- 330
Cdd:cd02874 208 REKILLGIPLYGYDWTLPYKKGGKAST-----------------ISPQQAINLAkryGAEIQYDEEAQSPFFRyVDEQgr 270
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622828392 331 --WVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDD 364
Cdd:cd02874 271 rhEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLED 306
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
46-272 |
1.56e-17 |
|
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an uncharacterized bacterial member of the family 18 glycosyl hydrolases with homologs found in Flavobacterium, Stigmatella, and Pseudomonas.
Pssm-ID: 119362 [Multi-domain] Cd Length: 253 Bit Score: 82.11 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 46 VDPSLCTHLIYAFAGMTNHQLSTIEWNDETLYQEFNGRKKMNpkLKTLLAIGGWNFGTqrFTDMVATANNRQTFVNSAIR 125
Cdd:cd06545 18 IDFSKLTHINLAFANPDANGTLNANPVRSELNSVVNAAHAHN--VKILISLAGGSPPE--FTAALNDPAKRKALVDKIIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 126 FLRKYGFDGLDLDWEypgsrgSPAIDKERFTALVQDLANAFQqeaqtsgKERLLLSAAVPAGrtyvDAGYEVDKIARNLD 205
Cdd:cd06545 94 YVVSYNLDGIDVDLE------GPDVTFGDYLVFIRALYAALK-------KEGKLLTAAVSSW----NGGAVSDSTLAYFD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828392 206 FVNLMAYDFHGSWEKVTGHnsplykrQEESGAAASLNVDaavqMWLQKG-TPASKLILGMPTYGRSFT 272
Cdd:cd06545 157 FINIMSYDATGPWWGDNPG-------QHSSYDDAVNDLN----YWNERGlASKDKLVLGLPFYGYGFY 213
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
419-466 |
5.47e-14 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 65.93 E-value: 5.47e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1622828392 419 FCQGKADGLYPNPRERSSFYSCAGGRLFQQSCPAGLVFSSSCKCCTWN 466
Cdd:smart00494 2 ECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
114-367 |
3.92e-13 |
|
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.
Pssm-ID: 119354 [Multi-domain] Cd Length: 358 Bit Score: 70.54 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 114 NNRQTFVNSAIRFLRKYGFDGLDLDWEYPGSRGSPAIDKerFTALVQDLANAFQQEAQTSGkerllLSAAVPAGRTYVD- 192
Cdd:cd02875 95 TYRTQWIQQKVELAKSQFMDGINIDIEQPITKGSPEYYA--LTELVKETTKAFKKENPGYQ-----ISFDVAWSPSCIDk 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 193 AGYEVDKIARNLDFVNLMAYDfHGS--WEKV--TGHNSPLykrqeesgaaasLNVDAAVQMWLQKGTPASKLILGMPTYG 268
Cdd:cd02875 168 RCYDYTGIADASDFLVVMDYD-EQSqiWGKEciAGANSPY------------SQTLSGYNNFTKLGIDPKKLVMGLPWYG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 269 RSFTLAS----------PSDTRVGAPAT-GSGTPGPFTKEGGMLAyyevcSWKGATKQRIQDQEVPYIFRDNQ----WVG 333
Cdd:cd02875 235 YDYPCLNgnledvvctiPKVPFRGANCSdAAGRQIPYSEIMKQIN-----SSIGGRLWDSEQKSPFYNYKDKQgnlhQVW 309
|
250 260 270
....*....|....*....|....*....|....
gi 1622828392 334 FDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAG 367
Cdd:cd02875 310 YDNPQSLSIKVAYAKNLGLKGIGMWNGDLLDYSG 343
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
420-465 |
1.05e-11 |
|
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.
Pssm-ID: 426342 [Multi-domain] Cd Length: 53 Bit Score: 59.73 E-value: 1.05e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1622828392 420 CQGKADGLYPNPRERSSFYSCAGGRLFQQSCPAGLVFSSSCKCCTW 465
Cdd:pfam01607 1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
|
|
| GH18_SI-CLP |
cd02876 |
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ... |
84-288 |
3.20e-10 |
|
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein of unknown function that interacts with the endocytic/sorting transmembrane receptor stabilin-1 and is secreted from the lysosome. SI-CLP has a glycosyl hydrolase family 18 (GH18) domain but lacks a chitin-binding domain. The catalytic amino acids of the GH18 domain are not conserved in SI-CLP, similar to the chitolectins YKL-39, YKL-40, and YM1/2. Human SI-CLP is sorted to late endosomes and secretory lysosomes in alternatively activated macrophages.
Pssm-ID: 119355 [Multi-domain] Cd Length: 318 Bit Score: 61.17 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 84 KKMNPKLKTL--LAIGGWNFGtqrftDMVATANN---RQTFVNSAIRFLRKYGFDGLDLD-WEYPGSRGSPAIDKERFTa 157
Cdd:cd02876 61 RKANKNIKILprVLFEGWSYQ-----DLQSLLNDeqeREKLIKLLVTTAKKNHFDGIVLEvWSQLAAYGVPDKRKELIQ- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 158 LVQDLANAFQqeaqtsgKERLLLSAAVPAGRTYVDAGYEV-----DKIARNLDFVNLMAYDFHGSWEKvtGHNSPLYKrq 232
Cdd:cd02876 135 LVIHLGETLH-------SANLKLILVIPPPREKGNQNGLFtrkdfEKLAPHVDGFSLMTYDYSSPQRP--GPNAPLSW-- 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828392 233 eesgaaaslnVDAAVQMWLQKGTP-ASKLILGMPTYGRSFTLaspsdTRVGAPATGS 288
Cdd:cd02876 204 ----------VRSCLELLLPESGKkRAKILLGLNFYGNDYTL-----PGGGGAITGS 245
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
24-212 |
1.04e-08 |
|
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
Pssm-ID: 119350 [Multi-domain] Cd Length: 312 Bit Score: 56.57 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 24 LVCYFTNWAQYrqGEARFLPKDVDPSLCTHLIYAFAGMTNHQLSTIEWNDETLY-----QEF-NGRKKMNPK-LKTLLAI 96
Cdd:cd02871 3 LVGYWHNWDNG--AGSGRQDLDDVPSKYNVINVAFAEPTSDGGGEVTFNNGSSPggyspAEFkADIKALQAKgKKVLISI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 97 GGwnfgtQRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEYpGSRGSPAIDKerftalVQDLANAFQQEAQTSGKE 176
Cdd:cd02871 81 GG-----ANGHVDLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLES-GSNPLNATPV------ITNLISALKQLKDHYGPN 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622828392 177 rLLLSAAvP---------AGRTYVDAGYE--VDKIARNLDFVNLMAY 212
Cdd:cd02871 149 -FILTMA-PetpyvqggyAAYGGIWGAYLplIDNLRDDLTWLNVQYY 193
|
|
| GH18_trifunctional |
cd06549 |
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ... |
85-364 |
4.46e-08 |
|
GH18 domain of an uncharacterized family of bacterial proteins, which share a common three-domain architecture: an N-terminal glycosyl hydrolase family 18 (GH18) domain, a glycosyl transferase family 2 domain, and a C-terminal polysaccharide deacetylase domain.
Pssm-ID: 119366 [Multi-domain] Cd Length: 298 Bit Score: 54.34 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 85 KMNPKLKTL-LAIGGWNFGTQRFTDMVATANNRQTFVNSAIRFLRKYGFDGLDLDWEypgsrGSPAIDKERFTALVQDLA 163
Cdd:cd06549 57 KAHPKVLPLvQNISGGAWDGKNIARLLADPSARAKFIANIAAYLERNQADGIVLDFE-----ELPADDLPKYVAFLSELR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 164 NAFqqeaqtsGKERLLLSAAVPAGrtyvDAGYEVDKIARNLDFVNLMAYDFHGswekVTGHNSPLYKRQeesgaAASLNV 243
Cdd:cd06549 132 RRL-------PAQGKQLTVTVPAD----EADWNLKALARNADKLILMAYDEHY----QGGAPGPIASQD-----WFESNL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 244 DAAVqmwlqKGTPASKLILGMPTYGRSFTlaspsdtrvgapaTGSGTPGPFTKEGGMLAYYEvcswkGATKQRIQDQEVP 323
Cdd:cd06549 192 AQAV-----KKLPPEKLIVALGSYGYDWT-------------KGGNTKAISSEAAWLLAAHA-----SAAVKFDDKASNA 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622828392 324 YIF-------RDNQWvgFDDVESFKTKVSYLKQKGLGGAMVWALDLDD 364
Cdd:cd06549 249 TYFfyddegvSHEVW--MLDAVTLFNQLKAVQRLGPAGVALWRLGSED 294
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
91-168 |
2.23e-07 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 53.22 E-value: 2.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828392 91 KTLLAIGGWNfGTQRftdmVATANNRQTFVNSAIRFLRKYGFDGLDLDWEyPGSRGSPAIDKErfTALVQDLANAFQQ 168
Cdd:COG3469 290 KVLLSIGGAN-GTVQ----LNTAAAADNFVNSVIALIDEYGFDGLDIDLE-GGSNSLNAGDTD--TPVITNLISALKQ 359
|
|
| GH18_EndoS-like |
cd06542 |
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ... |
129-229 |
8.95e-04 |
|
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
Pssm-ID: 119359 Cd Length: 255 Bit Score: 40.82 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 129 KYGFDGLDLDWEY-PGSRGSPAI-DKERFTALVQDLANAFQqeaqtsgkerlllsaavPAGRT---YVDAGYEVDKIARN 203
Cdd:cd06542 102 KYGLDGVDFDDEYsGYGKNGTSQpSNEAFVRLIKELRKYMG-----------------PTDKLltiDGYGQALSNDGEEV 164
|
90 100
....*....|....*....|....*.
gi 1622828392 204 LDFVNLMAYDFHGSWEKVTGHNSPLY 229
Cdd:cd06542 165 SPYVDYVIYQYYGSSSSSTQRNWNTN 190
|
|
| GH18_narbonin |
cd06544 |
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ... |
46-140 |
4.00e-03 |
|
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons with unknown function. Narbonin has a glycosyl hydrolase family 18 (GH18) domain without the conserved catalytic residues and with no known enzymatic activity. Narbonin amounts to up to 3% of the total seed globulins of mature seeds and was thought to be a storage protein but was found to degrade too slowly during germination. This family also includes the VfNOD32 nodulin from Vicia faba.
Pssm-ID: 119361 Cd Length: 253 Bit Score: 38.89 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828392 46 VDPSLCTHLIYAFA-GMTNHQLST-----IEWNDETLYQE-FNGRKKMNPKLKTLLAIGGWNFGTQ-RFTDmvaTANNrQ 117
Cdd:cd06544 20 INPKVEFHFILSFAiDYDTESNPTngkfnPYWDTENLTPEaVKSIKAQHPNVKVVISIGGRGVQNNpTPFD---PSNV-D 95
|
90 100
....*....|....*....|....*..
gi 1622828392 118 TFVNSAIRFL----RKYGFDGLDLDWE 140
Cdd:cd06544 96 SWVSNAVSSLtsiiQTYNLDGIDIDYE 122
|
|
| |
